EC Number   |
Application |
Reference |
|---|
    3.2.1.21 | analysis |
comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major |
679943 |
| 3.2.1.21 | biofuel production |
biodegradation of lignocellulosic biomass involves a concerted attack by several enzymes, including beta-glucosidases as key component. Current methodologies for biomass conversion to biofuels employ physical and/or chemical pretreatments that disrupt the lignocellulosic biomass in plant cell walls in combination with enzymatic hydrolysis of the cellulose to produce free sugars. Thus, stable cellulolytic enzymes with high enzymatic activity in pretreatment biomass conditions, including high temperatures and acidic conditions, are essential at an industrial scale production. These two features makes beta-glucosidase TpBGL1 to be of significant biotechnological interest |
-, 746720 |
| 3.2.1.21 | biofuel production |
biodegradation of lignocellulosic biomass involves a concerted attack by several enzymes, including beta-glucosidases as key component. Current methodologies for biomass conversion to biofuels employ physical and/or chemical pretreatments that disrupt the lignocellulosic biomass in plant cell walls in combination with enzymatic hydrolysis of the cellulose to produce free sugars. Thus, stable cellulolytic enzymes with high enzymatic activity in pretreatment biomass conditions, including high temperatures and acidic conditions, are essential at an industrial scale production. These two features makes beta-glucosidase TpBGL3 to be of significant biotechnological interest |
-, 746720 |
| 3.2.1.21 | biofuel production |
the saccharification yield of rice straw using Trichoderma reesei cellulase is improved by the addition of MeBglD2. These results show that MeBglD2 can be used to improve plant biomass saccharification, because both substrates and products can activate its enzymatic activity |
749691 |
| 3.2.1.21 | biotechnology |
immobilization of the enzyme on gelatin, overview, the very stable gelatin-immobilized enzyme can be used in continuous synthesis of beta-glucosides by transglucosylation |
664370 |
| 3.2.1.21 | biotechnology |
production of isoflavone aglycones by the enzyme. Isoform BGL1 shows broad substrate specificity to various isoflavone glycosides, the residual ratio is reached to 6.2% of the total amount of isoflavone glycosides and the hydrolysis reaction is almost finished within 48 h |
695794 |
| 3.2.1.21 | biotechnology |
the beta-glucosidase has a potential for biotechnological applications in the bioconversion of lignocellulosic materials |
705104 |
| 3.2.1.21 | biotechnology |
the bifunctional beta-glucosidase/xylosidase can be used in simultaneous saccharification of cellulose and xylan into fermenantable glucose and xylose |
718065 |
| 3.2.1.21 | biotechnology |
the enzyme might be useful as biocatalyst in the synthesis of glyco-conjugates, overview |
663728 |
| 3.2.1.21 | degradation |
a 3.43fold synergistic effect by combining with Trichoderma reesei cellulases is observed |
-, 742093 |
